Results 61 to 70 of about 4,605 (211)

Cloning and developmental expression of zebrafish GTP cyclohydrolase I

Mechanisms of Development, 2001
GTP cyclohydrolase I (GCH) catalyses the conversion of GTP to dihydroneopterin triphosphate, initiating the pteridine pathway. The final product tetrahydrobiopterin (H4biopterin) is the cofactor for neurotransmitter synthesis and for tyrosine supply during melanogenesis. Sepiapterin accumulates as a pigment.
Pelletier, Isabelle, Bally-Cuif, Laure, Ziegler, Irmgard   +2 more
openaire   +2 more sources

Biochemical Characterization of Oligomerization of Escherichia coli GTP Cyclohydrolase I [PDF]

BMB Reports, 2002
GTP cyclohydrolase I (E.C. 3.5.4.16) is a homodecameric protein that catalyzes the conversion of GTP to 7,8- dihydroneopterin triphosphate (H(2)NTP), the initial step in the biosynthesis of pteridines. It was proposed that the enzyme complex could be composed of a dimer of two pentamers, or a pentamer of tightly associated dimers; then the active site ...
Soojin, Lee, Chiyoung, Ahn, Eungsik, Park, Deog Su, Hwang, Jeongbin, Yim   +4 more
openaire   +2 more sources

Ferroptosis: The Demise of Cells Through Phospholipid Peroxidation

Advanced Science, Volume 13, Issue 23, 23 April 2026.
The relative abundance of peroxidation‐resistant monounsaturated fatty acids (MUFAs) vs. peroxidation‐sensitive polyunsaturated fatty acids (PUFAs) incorporated into phospholipid (PL) is a key determinant of ferroptosis sensitivity, as the peroxidation of PL PUFA acyl chains (PUFA‐PL) disrupts membrane integrity, causing ferroptotic cell death ...
Shaojie Cui, Jin Ye
wiley   +1 more source

Biosynthesis of Methanopterin in Methanobacterium thermoautotrophicum

Pteridines, 1994
The early steps in the biosynthesis of methanopterin in Methanobacterium thennoautotrophicum were analyzed by in vivo incorporation experiments of 13C labeled precursors and by enzymatic studies.
Eisenreich Wolfgang, Bacher Adelbert
doaj   +1 more source

Discovery of a New Prokaryotic Type I GTP Cyclohydrolase Family [PDF]

Journal of Biological Chemistry, 2006
GTP cyclohydrolase I (GCYH-I) is the first enzyme of the de novo tetrahydrofolate biosynthetic pathway present in bacteria, fungi, and plants, and encoded in Escherichia coli by the folE gene. It is also the first enzyme of the biopterin (BH4) pathway in Homo sapiens, where it is encoded by a homologous folE gene.
Basma, El Yacoubi, Shilah, Bonnett, Jessica N, Anderson, Manal A, Swairjo, Dirk, Iwata-Reuyl, Valérie, de Crécy-Lagard   +5 more
openaire   +2 more sources

Unraveling Chronic Pain: From Mechanisms and Risks to Diagnosis and Treatment

MedComm, Volume 7, Issue 4, April 2026.
Chronic pain arises through distinct molecular pathways categorized into nociceptive, neuropathic, and nociplastic types. Nociceptive pain begins with TRP channel activation in peripheral nociceptors, signaling via Aδ‐ and C‐fibers through the spinal dorsal horn and spinothalamic tracts to the brain, regulated by descending inhibition and involving ...
Xiaofeng Dai, Chongxiang Wang, Ping Jiang, Xiaopeng Mei   +3 more
wiley   +1 more source

When Pathways Converge: Iron, Lipid Peroxidation, and α‐Synuclein in Ferroptosis‐Driven Dopaminergic Neurodegeneration

Journal of Neurochemistry, Volume 170, Issue 4, April 2026.
Dopaminergic neurons are particularly susceptible to ferroptosis. Pacemaking activity–driven calcium (Ca2+) influx increases metabolic demand and reactive oxygen species (ROS) production, promoting iron release from aconitase. Alpha‐synuclein (α‐syn) enhances iron uptake via transferrin receptor 1 (TfR1) and exhibits ferrireductase activity, converting
Carmem L. Sperlich, Brent R. Stockwell, Marcelo Farina   +2 more
wiley   +1 more source

Rat GTP cyclohydrolase I is a homodecameric protein complex containing high-affinity calcium-binding sites

, 1998
Recombinant rat liver GTP cyclohydrolase I has been prepared by heterologous gene expression in Escherichia coli and characterized by biochemical and biophysical methods.
Aebi, U., Werner, Ernst R., Steinmetz, Michel O., Christen, Urs, Wolpensinger, Bettina, Kammerer, Richard A., Wachter, H., Aebi, Ueli, Engel, Andreas, Werner, E. R., Christen, U., Lustig, A., Engel, A., Kammerer, R. A., Steinmetz, M. O., Plüss, Christoph, Lustig, Ariel, Pluss, C., Wolpensinger, B., Pfeilschifter, Josef, Wachter, Helmut, Pfeilschifter, J.   +21 more
core   +1 more source

Regulation of GTP cyclohydrolase I by alternative splicing in mononuclear cells [PDF]

Biochemical and Biophysical Research Communications, 2003
GTP cyclohydrolase I (GCH, EC 3.5.4.16) regulates the level of tetrahydrobiopterin and in turn the activities of nitric oxide synthase and aromatic amino acid hydroxylases. Type II GCH mRNA, an alternatively spliced species abundant in blood cells, encodes a truncated and nonfunctional protein.
Wuh-Liang, Hwu, Hui-Ying, Yeh, Shu-Wen, Fang, Hao-Sen, Chiang, Yu-Wei, Chiou, Yu-May, Lee   +5 more
openaire   +2 more sources

The Genetic Basis of Color Polymorphism in the Orb‐Web Spider Gasteracantha cancriformis

Ecology and Evolution, Volume 16, Issue 3, March 2026.
This study investigates the genetic basis of coloration in the polymorphic spider Gasteracantha cancriformis using RNA‐seq data from different female color morphs. We assembled a reference transcriptome and identified differentially expressed genes associated with known pigmentation pathways, including carotenoids, melanin, ommochromes, and pteridines.
Paula Torres‐Quintero, Carolina Pardo‐Díaz, Fabian Salgado‐Roa, Camilo Salazar   +3 more
wiley   +1 more source